ID KTHY_PYRAB Reviewed; 205 AA.
AC Q9V1E9; G8ZGI2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Probable thymidylate kinase;
DE EC=2.7.4.9;
DE AltName: Full=dTMP kinase;
GN Name=tmk; OrderedLocusNames=PYRAB04780; ORFNames=PAB0319;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528,
CC ChEBI:CHEBI:456216; EC=2.7.4.9;
CC -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
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DR EMBL; AJ248284; CAB49400.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69861.1; -; Genomic_DNA.
DR PIR; A75165; A75165.
DR RefSeq; WP_010867602.1; NC_000868.1.
DR AlphaFoldDB; Q9V1E9; -.
DR SMR; Q9V1E9; -.
DR STRING; 272844.PAB0319; -.
DR GeneID; 1495374; -.
DR KEGG; pab:PAB0319; -.
DR PATRIC; fig|272844.11.peg.505; -.
DR eggNOG; arCOG01891; Archaea.
DR HOGENOM; CLU_049131_1_3_2; -.
DR OrthoDB; 43083at2157; -.
DR PhylomeDB; Q9V1E9; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01672; TMPK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00165; Thymidylate_kinase; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039430; Thymidylate_kin-like_dom.
DR InterPro; IPR018095; Thymidylate_kin_CS.
DR InterPro; IPR018094; Thymidylate_kinase.
DR NCBIfam; TIGR00041; DTMP_kinase; 1.
DR PANTHER; PTHR10344; THYMIDYLATE KINASE; 1.
DR PANTHER; PTHR10344:SF4; THYMIDYLATE KINASE; 1.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide biosynthesis; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..205
FT /note="Probable thymidylate kinase"
FT /id="PRO_0000155392"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 205 AA; 23513 MW; 1B011D41DEAC5115 CRC64;
MRGYFVVLEG IDGSGKTTQA KLLAEWFEEQ GWDVLLTKEP TDTEFGRLIR ELVLKNSIID
GSRISYEAEA LLFAADRAEH VKKVILPALE KGKVVICDRY LYSSLAYQWA RGLSLEWLMQ
INSFAPRPDL AILLDLPVKE SIRRTKARGN MSEFDKLLEL QRKVRMNYLK LAEMFKEMRI
VNAMASVEEV HEDIVALVKH ELLGL
//
